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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 382, Issue 6

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Legumain Forms from Plants and Animals Differ in Their Specificity

Vitalie I. Rotari / Pam M. Dando / Alan J. Barrett
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2001.119

Abstract

We purified forms of legumain from a plant source (seeds of kidney bean, Phaseolus vulgaris) and a mammal (kidney of pig, Sus scropha) for comparison of their properties. Both forms were found to be stable only under moderately acidic pH conditions, and were maximally active at about pH 6; the plant enzyme was somewhat less stable and had a slightly higher pH optimum. With benzyloxycarbonylXaa AlaAsnaminomethylcoumarylamide substrates, the two forms of legumain showed distinctly different specificities for the P3 residue, the plant legumain preferring amino acids with bulky hydrophobic side chains because of lower K values. Both forms of legumain were highly specific for hydrolysis of asparaginyl bonds in the arylamide substrates and in neurotensin. Aspartyl bonds were hydrolysed about 100-fold more slowly with lower pH optima. Potential substrates containing other amino acids structurally similar to asparagine were not hydrolysed. There were clear differences in specificity of hydrolysis of protein substrates. The plant legumain differed from pig legumain in its action on tetanus toxoid Cfragment, cleaving at Asn[97] but not at Asn[337], and produced more extensive digestion of phaseolin. The plant form of legumain was much more weakly inhibited by eggwhite cystatin than was the mammalian form.

About the article

Published Online: 2005-06-01

Published in Print: 2001-06-27


Citation Information: Biological Chemistry, Volume 382, Issue 6, Pages 953–959, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2001.119.

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